7zrd: Difference between revisions
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[7zrd]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7ZRD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7ZRD FirstGlance]. <br> | <table><tr><td colspan='2'>[[7zrd]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7ZRD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7ZRD FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CDL:CARDIOLIPIN'>CDL</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=SEP:PHOSPHOSERINE'>SEP</scene>, <scene name='pdbligand=VO4:VANADATE+ION'>VO4</scene></td></tr> | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.3Å</td></tr> | ||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CDL:CARDIOLIPIN'>CDL</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=SEP:PHOSPHOSERINE'>SEP</scene>, <scene name='pdbligand=VO4:VANADATE+ION'>VO4</scene></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=7zrd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7zrd OCA], [https://pdbe.org/7zrd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7zrd RCSB], [https://www.ebi.ac.uk/pdbsum/7zrd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7zrd ProSAT]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=7zrd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7zrd OCA], [https://pdbe.org/7zrd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7zrd RCSB], [https://www.ebi.ac.uk/pdbsum/7zrd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7zrd ProSAT]</span></td></tr> | ||
</table> | </table> | ||
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<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
KdpFABC is a high-affinity prokaryotic K | KdpFABC is a high-affinity prokaryotic K(+) uptake system that forms a functional chimera between a channel-like subunit (KdpA) and a P-type ATPase (KdpB). At high K(+) levels, KdpFABC needs to be inhibited to prevent excessive K(+) accumulation to the point of toxicity. This is achieved by a phosphorylation of the serine residue in the TGES(162) motif in the A domain of the pump subunit KdpB (KdpB(S162-P)). Here, we explore the structural basis of inhibition by KdpB(S162) phosphorylation by determining the conformational landscape of KdpFABC under inhibiting and non-inhibiting conditions. Under turnover conditions, we identified a new inhibited KdpFABC state that we termed E1P tight, which is not part of the canonical Post-Albers transport cycle of P-type ATPases. It likely represents the biochemically described stalled E1P state adopted by KdpFABC upon KdpB(S162) phosphorylation. The E1P tight state exhibits a compact fold of the three cytoplasmic domains and is likely adopted when the transition from high-energy E1P states to E2P states is unsuccessful. This study represents a structural characterization of a biologically relevant off-cycle state in the P-type ATPase family and supports the emerging discussion of P-type ATPase regulation by such states. | ||
Inhibited KdpFABC transitions into an E1 off-cycle state.,Silberberg JM, Stock C, Hielkema L, Corey RA, Rheinberger J, Wunnicke D, Dubach VRA, Stansfeld PJ, Hanelt I, Paulino C Elife. 2022 Oct 18;11 | Inhibited KdpFABC transitions into an E1 off-cycle state.,Silberberg JM, Stock C, Hielkema L, Corey RA, Rheinberger J, Wunnicke D, Dubach VRA, Stansfeld PJ, Hanelt I, Paulino C Elife. 2022 Oct 18;11:e80988. doi: 10.7554/eLife.80988. PMID:36255052<ref>PMID:36255052</ref> | ||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||